FBP1 as a key regulator of focal adhesion kinase-mediated hepatic stellate cell activation: Multi-omics and experimental validation

Figure 6 Fructose-1,6-bisphosphatase 1 recombinant protein (HY-P70275) inhibits the activation, migration, and aerobic glycolysis of hepatic stellate cells. A: At concentrations of 12.5 ng/mL, 25 ng/mL, 50 ng/mL, and 100 ng/mL of fructose-1,6-bisphosphatase 1 (FBP1) recombinant protein, Western blot (WB) analysis was conducted to detect the expression of FBP1, collagen type 1, alpha 1 (COL1A1), and alpha smooth muscle actin (α-SMA) proteins, which are markers of liver fibrosis, with β-actin serving as the internal control; B: Grayscale value statistics were performed for each protein group, and statistical significance relative to the control (dimethyl sulfoxide [DMSO]) group was evaluated; C: At the same concentrations of FBP1 recombinant protein, WB analysis was used to detect the expression of aerobic glycolysis enzymes, including lactate dehydrogenase A (LDHA), hexokinase 2 (HK2), phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 (PFKFB3), and pyruvate kinase M2 (PKM2), with β-actin as the internal control; D: Grayscale value analysis was conducted for each proteome, and statistical significance relative to the control (DMSO) group was evaluated; E: At a concentration of 100 ng/mL of FBP1 recombinant protein, the migration ability of LX-2 cells in each group was assessed using a wound healing assay; F: The cell migration area relative to the control (DMSO) group was evaluated; G: At a concentration of 100 ng/mL of FBP1 recombinant protein, the migration ability of LX-2 cells in each group was assessed using a Transwell migration assay, observed under a light microscope at 100 × magnification; H: The number of cells that migrated through the membrane of the Transwell chamber relative to the control (DMSO) group was assessed. All data are from three independent samples. Data are represented as the mean ± SD. ^aNot significant; ^bP < 0.01, ^cP < 0.001, ^dP < 0.0001.